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. 1996 Mar;110(3):997–1005. doi: 10.1104/pp.110.3.997

Cool-temperature-induced chlorosis in rice plants.

R Yoshida 1, A Kanno 1, T Sato 1, T Kameya 1
PMCID: PMC157800  PMID: 8819872

Abstract

We have established an experimental system for mimicking the phenomenon of cool-temperature-induced chlorosis (CTIC) in rice plants (Oryza sativa L.). Rice seedlings were initially grown in darkness under cool-temperature conditions and then exposed to light and warm conditions to follow the expression of CTIC. Induction of CTIC in the sensitive cultivar (cv Surjamukhi) was bimodally dependent on the temperatures experienced during the initial growth in darkness. CTIC was maximally induced between 15 and 17 degrees C. A positive correlation was demonstrated between induction of CTIC and the growth activity of shoots during growth in darkness. Electrophoretic and immunoblot analysis revealed that accumulation of NADPH-protochlorophyllide oxidoreductase in plastids was also bimodally dependent on the temperatures during the growth in darkness with minimum accumulation between 15 and 17 degrees C, suggesting that the reduction of NADPH-protochlorophyllide oxidoreductase accumulation in plastids might be closely linked to a disturbance in transformations of plastids to etioplasts during the dark growth under the critical temperatures and thereby to the CTIC phenomenon. This was corroborated by electron microscopic observations. These results suggest that growth is one of the determining factors for the expression of CTIC phenotype in rice under cool temperature.

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Selected References

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  1. Apel K. The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Phytochrome-induced decrease of translatable mRNA coding for the NADPH: protochlorophyllide oxidoreductase. Eur J Biochem. 1981 Nov;120(1):89–93. doi: 10.1111/j.1432-1033.1981.tb05673.x. [DOI] [PubMed] [Google Scholar]
  2. Archer E. K., Keegstra K. Current views on chloroplast protein import and hypotheses on the origin of the transport mechanism. J Bioenerg Biomembr. 1990 Dec;22(6):789–810. doi: 10.1007/BF00786931. [DOI] [PubMed] [Google Scholar]
  3. Boffey S. A., Ellis J. R., Selldén G., Leech R. M. Chloroplast Division and DNA Synthesis in Light-grown Wheat Leaves. Plant Physiol. 1979 Sep;64(3):502–505. doi: 10.1104/pp.64.3.502. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  5. Dahlin C., Cline K. Developmental Regulation of the Plastid Protein Import Apparatus. Plant Cell. 1991 Oct;3(10):1131–1140. doi: 10.1105/tpc.3.10.1131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Forreiter C., Apel K. Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo). Planta. 1993;190(4):536–545. doi: 10.1007/BF00224793. [DOI] [PubMed] [Google Scholar]
  7. He Z. H., Li J., Sundqvist C., Timko M. P. Leaf Developmental Age Controls Expression of Genes Encoding Enzymes of Chlorophyll and Heme Biosynthesis in Pea (Pisum sativum L.). Plant Physiol. 1994 Oct;106(2):537–546. doi: 10.1104/pp.106.2.537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  9. Moran R., Porath D. Chlorophyll determination in intact tissues using n,n-dimethylformamide. Plant Physiol. 1980 Mar;65(3):478–479. doi: 10.1104/pp.65.3.478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Reinbothe S., Runge S., Reinbothe C., van Cleve B., Apel K. Substrate-dependent transport of the NADPH:protochlorophyllide oxidoreductase into isolated plastids. Plant Cell. 1995 Feb;7(2):161–172. doi: 10.1105/tpc.7.2.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Schulz R., Steinmüller K., Klaas M., Forreiter C., Rasmussen S., Hiller C., Apel K. Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. Mol Gen Genet. 1989 Jun;217(2-3):355–361. doi: 10.1007/BF02464904. [DOI] [PubMed] [Google Scholar]
  12. Spano A. J., He Z., Michel H., Hunt D. F., Timko M. P. Molecular cloning, nuclear gene structure, and developmental expression of NADPH: protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol Biol. 1992 Mar;18(5):967–972. doi: 10.1007/BF00019210. [DOI] [PubMed] [Google Scholar]
  13. Susek R. E., Ausubel F. M., Chory J. Signal transduction mutants of Arabidopsis uncouple nuclear CAB and RBCS gene expression from chloroplast development. Cell. 1993 Sep 10;74(5):787–799. doi: 10.1016/0092-8674(93)90459-4. [DOI] [PubMed] [Google Scholar]
  14. Tam J. P. Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proc Natl Acad Sci U S A. 1988 Aug;85(15):5409–5413. doi: 10.1073/pnas.85.15.5409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Wray W., Boulikas T., Wray V. P., Hancock R. Silver staining of proteins in polyacrylamide gels. Anal Biochem. 1981 Nov 15;118(1):197–203. doi: 10.1016/0003-2697(81)90179-2. [DOI] [PubMed] [Google Scholar]

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